Výsledky vyhledávání - "Nisha T. Palackal"

Fjord-region Benzo[g]chrysene-11,12-dihydrodiol and Benzo[c]phenanthrene-3,4-dihydrodiol as Substrates for Rat Liver Dihydrodiol Dehydrogenase (AKR1C9): Structural Basis for Stereochemical Preference

Autor: Trevor M. Penning, Carol A. Shultz, Ronald G. Harvey, Dipti Mangal, Ian A. Blair, Nisha T. Palackal

Publikováno v: Chemical Research in Toxicology. 21:668-677

This study demonstrates that benzo[g]chrysene-11,12-dihydrodiol (B[g]C-11,12-dihydrodiol) derived from the fjord-region parent hydrocarbon B[g]C is oxidized by rat AKR1C9 with a k c a t/ K m 100 times greater than that observed with the commonly stud

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::454dff842a8085080520e0afd37ddffb
https://doi.org/10.1021/tx7003695

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Activation of Polycyclic Aromatic Hydrocarbontrans-Dihydrodiol Proximate Carcinogens by Human Aldo-keto Reductase (AKR1C) Enzymes and Their Functional Overexpression in Human Lung Carcinoma (A549) Cells

Autor: Seon Hwa Lee, Ian A. Blair, Ronald G. Harvey, Trevor M. Penning, Nisha T. Palackal

Publikováno v: Journal of Biological Chemistry. 277:24799-24808

Polycyclic aromatic hydrocarbons (PAH) are environmental pollutants and suspected human lung carcinogens. In patients with non-small cell lung carcinoma, differential display shows that aldo-keto reductase (AKR1C) transcripts are dramatically overexp

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::e180fee223fb4243fda93cc21b3ab8c2
https://doi.org/10.1074/jbc.m112424200

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Human AKR1C Isoforms Oxidize the Potent Proximate Carcinogen 7,12-DMBA-3,4-diol in the Human Lung A549 Carcinoma Cell Line

Autor: Seon Hwa Lee, Ronald G. Harvey, Ian A. Blair, Nisha T. Palackal, Trevor M. Penning

Publikováno v: Polycyclic Aromatic Compounds. 22:801-810

Aldo-keto reductases (AKRs) oxidize structurally diverse PAH trans -dihydrodiols to yield reactive and redox active o -quinones. This study examined the ability of AKR1C2 and AKR1C4 to oxidize PAH trans -dihydrodiols of the benz[ a ]anthracene series

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::f9f4ec061b179be847585c37e62e6cac
https://doi.org/10.1080/10406630290103951

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Crystal Structure of Human Type III 3α-Hydroxysteroid Dehydrogenase/Bile Acid Binding Protein Complexed with NADP+ and Ursodeoxycholate

Autor: Nisha T. Palackal, Trevor M. Penning, Mitchell Lewis, Steven Stayrook, Ross H. Albert, Yi Jin

Publikováno v: Biochemistry. 40:10161-10168

The crystal structure of human type III 3alpha-hydroxysteroid dehydrogenase (HSD)/bile acid binding protein (AKR1C2) complexed with NADP(+) and 3alpha,7beta-dihydroxy-5beta-cholanic acid (ursodeoxycholate) at 3.0 A resolution is presented. Thus, the

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::0b4b8fbb6b2bd0906b46a4ae32503a17
https://doi.org/10.1021/bi010919a

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Polycyclic Aromatic HydrocarbonTrans-Dihydrodiol Specificity of four Recombinant Human Dihydrodiol Dehydrogenase Isoforms

Autor: Trevor M. Penning, Nisha T. Palackal, Ronald G. Harvey, Michael E. Burczynski

Publikováno v: Polycyclic Aromatic Compounds. 16:205-214

A major metabolic route of polycyclic aromatic hydrocarbon (PAH) activation proceeds through trans-dihydrodiol intermediates. We have previously shown that a member of the aldo-keto reductase (AKR) superfamily, rat liver dihydrodiol dehydrogenase (DD

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_________::521fb0a669382c80630ede34a321d221
https://doi.org/10.1080/10406639908020587

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The ubiquitous aldehyde reductase (AKR1A1) oxidizes proximate carcinogen trans-dihydrodiols to o-quinones: potential role in polycyclic aromatic hydrocarbon activation

Autor: Nisha T. Palackal, Ronald G. Harvey, Trevor M. Penning, Michael E. Burczynski

Publikováno v: Biochemistry. 40(36)

Polycyclic aromatic hydrocarbons (PAHs) are metabolized to trans-dihydrodiol proximate carcinogens by human epoxide hydrolase (EH) and CYP1A1. Human dihydrodiol dehydrogenase isoforms (AKR1C1-AKR1C4), members of the aldo-keto reductase (AKR) superfam

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7b8e28237ddb06c8d6cf6866265ead42
https://pubmed.ncbi.nlm.nih.gov/11535067

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Structure-function aspects and inhibitor design of type 5 17beta-hydroxysteroid dehydrogenase (AKR1C3)

Autor: Trevor M. Penning, Joseph M. Jez, Margaret Moore, Michael E. Burczynski, Kapila Ratnam, Hseuh Kung Lin, Nisha T. Palackal, Haiching Ma

Publikováno v: Molecular and cellular endocrinology. 171(1-2)

17beta-Hydroxysteroid dehydrogenase (17beta-HSD) type 5 has been cloned from human prostate and is identical to type 2 3alpha-HSD and is a member of the aldo-keto reductase (AKR) superfamily; it is formally AKR1C3. In vitro the homogeneous recombinan

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7c66a5af80a9725b6d7820b983aaf128
https://pubmed.ncbi.nlm.nih.gov/11165022

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The reactive oxygen species--and Michael acceptor-inducible human aldo-keto reductase AKR1C1 reduces the alpha,beta-unsaturated aldehyde 4-hydroxy-2-nonenal to 1,4-dihydroxy-2-nonene

Autor: Michael E. Burczynski, Gopishetty R. Sridhar, Nisha T. Palackal, Trevor M. Penning

Publikováno v: The Journal of biological chemistry. 276(4)

The human aldo-keto reductase AKR1C1 (20alpha(3alpha)-hydroxysteroid dehydrogenase) is induced by electrophilic Michael acceptors and reactive oxygen species (ROS) via a presumptive antioxidant response element (Burczynski, M. E., Lin, H. K., and Pen

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f667b9afda37e8de0358836b57328c0d
https://pubmed.ncbi.nlm.nih.gov/11060293

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